Structural Comparison between Collagen Isolated from Sea Cucumber Holothuria Parva and Calf Skin Collagen Type I

Aim and Collagen has a wide range of applications in biomedical, pharmaceutical, cosmetic, and food industries. Recently, isolation of collagen from marine species has been investiga ted. Collagen from cow has a risk for contamination from bovine spongiform encephalopathy (BSE), transmissible spongiform encephalopathy (TSE). The aim of this investigation is the extraction of collagen from body wall of sea cucumber (Holothuria parva) and comparison with collagen Type I. Pepsin-solubilized collagen (PSC) is extracted from body wall of sea cucumbers (Holothuria parva) and characterized by SDS-PAGE, DSC, FT-IR. SDS-PAGE shows that the major component consists of three α1 chains of approximately 130 kDa that is similar to calf skin collagen Type I with the same weight but different in α1 chains (α1)2 α2. The Tm of PSC is 46.940C therefore the thermal stability is lower than collagen Type I. Two peaks of transmission bands is determined by FT-IR including amide A (3420 cm-1) and amide I (1638 cm-1). Collagen isolated from the sea cucumber determines Type I and the thermal stability shows that it can be used as an alternative to mammalian collagen in the food and pharmaceutical industries. The thermal stability of PSC shows that it has lower content of Proline and Hydroxyproline in comparison with collagen Type I.